Sign in
ImmunologybioRxiv

Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

N. K. Hurlburt, Y.-H. Wan, A. B. Stuart, J. Feng, A. T. McGuire, L. Stamatatos, M. Pancera

Abstract

SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determined the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain (RBD). The structure reveals CV30s epitope overlaps with the human ACE2 receptor binding site thus providing the structural basis for its neutralization by preventing ACE2 binding.

PDFDOI

02 /Specification & Classification

Click any tag to browse matching papers

Reproducibility ledger

Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.

Sign in to file a reproducibility report.